A route to diastereomerically pure phenylglycine thioester peptides: crucial intermediates for investigating glycopeptide antibiotic biosynthesis

Julien Tailhades; Melanie Schoppet; Anja Greule; Madeleine Peschke; Clara Brieke; Max J Cryle

doi:10.1039/c7cc09409d

A route to diastereomerically pure phenylglycine thioester peptides: crucial intermediates for investigating glycopeptide antibiotic biosynthesis

Chem Commun (Camb). 2018 Feb 22;54(17):2146-2149. doi: 10.1039/c7cc09409d.

Authors

Julien Tailhades¹, Melanie Schoppet, Anja Greule, Madeleine Peschke, Clara Brieke, Max J Cryle

Affiliation

¹ EMBL Australia, Monash University, Clayton, Victoria 3800, Australia. [email protected].

PMID: 29423498
DOI: 10.1039/c7cc09409d

Abstract

Non-ribosomal peptides contain an array of amino acid building blocks that can present challenges for the synthesis of important intermediates. Here, we report the synthesis of glycopeptide antibiotic (GPA) thioester peptides that retains the crucial stereochemical purity of the terminal phenylglycine residue, which we show is essential for the enzymatic GPA cyclisation cascade.

MeSH terms

Anti-Bacterial Agents / chemical synthesis*
Anti-Bacterial Agents / chemistry
Anti-Bacterial Agents / metabolism
Biosynthetic Pathways
Chemistry Techniques, Synthetic / methods
Cyclization
Esterification
Glycine / analogs & derivatives*
Glycine / chemical synthesis
Glycine / metabolism
Glycopeptides / chemical synthesis*
Glycopeptides / chemistry
Glycopeptides / metabolism
Stereoisomerism
Sulfhydryl Compounds / chemical synthesis
Sulfhydryl Compounds / chemistry
Sulfhydryl Compounds / metabolism

Substances

Anti-Bacterial Agents
Glycopeptides
Sulfhydryl Compounds
Glycine